FBRL_YEAST
ID FBRL_YEAST Reviewed; 327 AA.
AC P15646; D6VRX5; P89890;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:24352239};
DE AltName: Full=Histone-glutamine methyltransferase;
DE AltName: Full=U3 small nucleolar RNA-associated protein NOP1;
DE Short=Nucleolar protein 1 {ECO:0000303|PubMed:2298745, ECO:0000303|PubMed:2686980};
DE Short=U3 snoRNA-associated protein NOP1;
GN Name=NOP1 {ECO:0000303|PubMed:2298745, ECO:0000303|PubMed:2686980};
GN Synonyms=LOT3; OrderedLocusNames=YDL014W; ORFNames=D2870;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 264-270 AND 298-310,
RP FUNCTION, INTERACTION WITH SNORNAS, AND SUBCELLULAR LOCATION.
RX PubMed=2686980; DOI=10.1002/j.1460-2075.1989.tb08584.x;
RA Schimmang T., Tollervey D., Kern H., Frank R., Hurt E.C.;
RT "A yeast nucleolar protein related to mammalian fibrillarin is associated
RT with small nucleolar RNA and is essential for viability.";
RL EMBO J. 8:4015-4024(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 112-142; 157-181 AND
RP 211-231, AND SUBCELLULAR LOCATION.
RX PubMed=2298745; DOI=10.1016/s0021-9258(19)39963-6;
RA Henriquez R., Blobel G., Aris J.P.;
RT "Isolation and sequencing of NOP1. A yeast gene encoding a nucleolar
RT protein homologous to a human autoimmune antigen.";
RL J. Biol. Chem. 265:2209-2215(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=1825809; DOI=10.1002/j.1460-2075.1991.tb07984.x;
RA Tollervey D., Lehtonen H., Carmo-Fonseca M., Hurt E.C.;
RT "The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-
RT rRNA processing in yeast.";
RL EMBO J. 10:573-583(1991).
RN [6]
RP INTERACTION WITH SOF1.
RX PubMed=8508778; DOI=10.1002/j.1460-2075.1993.tb05910.x;
RA Jansen R., Tollervey D., Hurt E.C.;
RT "A U3 snoRNP protein with homology to splicing factor PRP4 and G beta
RT domains is required for ribosomal RNA processing.";
RL EMBO J. 12:2549-2558(1993).
RN [7]
RP INTERACTION WITH SIK1 AND NOP58.
RX PubMed=9372940; DOI=10.1128/mcb.17.12.7088;
RA Gautier T., Berges T., Tollervey D., Hurt E.;
RT "Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and
RT are required for ribosome biogenesis.";
RL Mol. Cell. Biol. 17:7088-7098(1997).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12215523; DOI=10.1128/mcb.22.19.6663-6668.2002;
RA Galardi S., Fatica A., Bachi A., Scaloni A., Presutti C., Bozzoni I.;
RT "Purified box C/D snoRNPs are able to reproduce site-specific 2'-O-
RT methylation of target RNA in vitro.";
RL Mol. Cell. Biol. 22:6663-6668(2002).
RN [9]
RP INTERACTION WITH MPP10 AND SNORNA U3, AND IDENTIFICATION IN SSU PROCESSOME
RP BY MASS SPECTROMETRY.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [10]
RP SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
RX PubMed=12756332; DOI=10.1261/rna.5020803;
RA Xu C., Henry P.A., Setya A., Henry M.F.;
RT "In vivo analysis of nucleolar proteins modified by the yeast arginine
RT methyltransferase Hmt1/Rmt1p.";
RL RNA 9:746-759(2003).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [12]
RP METHYLATION AT ARG-16; ARG-22; ARG-30; ARG-34; ARG-40; ARG-48; ARG-52;
RP ARG-58; ARG-70; ARG-73 AND ARG-81.
RX PubMed=23865587; DOI=10.1021/pr400556c;
RA Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine.";
RL J. Proteome Res. 12:3884-3899(2013).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-87; GLU-103; ALA-175
RP AND PRO-219.
RX PubMed=24352239; DOI=10.1038/nature12819;
RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA Nielsen M.L., Kouzarides T.;
RT "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT modification.";
RL Nature 505:564-568(2014).
RN [14]
RP METHYLATION AT ARG-48; ARG-52; ARG-58; ARG-70; ARG-73 AND ARG-81.
RX PubMed=26081071; DOI=10.1002/pmic.201500075;
RA Yagoub D., Hart-Smith G., Moecking J., Erce M.A., Wilkins M.R.;
RT "Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively
RT methylated and are substrates of the arginine methyltransferase Hmt1p.";
RL Proteomics 15:3209-3218(2015).
RN [15]
RP METHYLATION AT ARG-70; ARG-73 AND ARG-81.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [16]
RP METHYLATION AT ARG-8; ARG-12; ARG-22; ARG-26; ARG-58; ARG-62; ARG-66;
RP ARG-70; ARG-73 AND ARG-81.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
RN [17] {ECO:0007744|PDB:5WLC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS).
RX PubMed=28945246; DOI=10.1038/nsmb.3472;
RA Barandun J., Chaker-Margot M., Hunziker M., Molloy K.R., Chait B.T.,
RA Klinge S.;
RT "The complete structure of the small-subunit processome.";
RL Nat. Struct. Mol. Biol. 24:944-953(2017).
RN [18] {ECO:0007744|PDB:5WYJ, ECO:0007744|PDB:5WYK}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS).
RX PubMed=28244370; DOI=10.7554/elife.22086;
RA Sun Q., Zhu X., Qi J., An W., Lan P., Tan D., Chen R., Wang B., Zheng S.,
RA Zhang C., Chen X., Zhang W., Chen J., Dong M.Q., Ye K.;
RT "Molecular architecture of the 90S small subunit pre-ribosome.";
RL Elife 6:0-0(2017).
RN [19] {ECO:0007744|PDB:6ND4}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS).
RX PubMed=31206356; DOI=10.7554/elife.45185;
RA Hunziker M., Barandun J., Buzovetsky O., Steckler C., Molina H., Klinge S.;
RT "Conformational switches control early maturation of the eukaryotic small
RT ribosomal subunit.";
RL Elife 8:0-0(2019).
RN [20] {ECO:0007744|PDB:6ZQA, ECO:0007744|PDB:6ZQB, ECO:0007744|PDB:6ZQC, ECO:0007744|PDB:6ZQD, ECO:0007744|PDB:6ZQE}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS).
RX PubMed=32943521; DOI=10.1126/science.abb4119;
RA Cheng J., Lau B., La Venuta G., Ameismeier M., Berninghausen O., Hurt E.,
RA Beckmann R.;
RT "90S pre-ribosome transformation into the primordial 40S subunit.";
RL Science 369:1470-1476(2020).
RN [21] {ECO:0007744|PDB:6LQP, ECO:0007744|PDB:6LQQ, ECO:0007744|PDB:6LQR, ECO:0007744|PDB:6LQS, ECO:0007744|PDB:6LQT, ECO:0007744|PDB:6LQU, ECO:0007744|PDB:6LQV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS).
RX PubMed=32943522; DOI=10.1126/science.aba9690;
RA Du Y., An W., Zhu X., Sun Q., Qi J., Ye K.;
RT "Cryo-EM structure of 90S small ribosomal subunit precursors in transition
RT states.";
RL Science 369:1477-1481(2020).
RN [22] {ECO:0007744|PDB:7AJT, ECO:0007744|PDB:7AJU}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS).
RX PubMed=33326748; DOI=10.1016/j.molcel.2020.11.009;
RA Lau B., Cheng J., Flemming D., La Venuta G., Berninghausen O., Beckmann R.,
RA Hurt E.;
RT "Structure of the Maturing 90S Pre-ribosome in Association with the RNA
RT Exosome.";
RL Mol. Cell 81:293-303(2021).
RN [23] {ECO:0007744|PDB:6ZDT}
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 83-327.
RX PubMed=33483369; DOI=10.1261/rna.077396.120;
RA Hoefler S., Lukat P., Blankenfeldt W., Carlomagno T.;
RT "High-resolution structure of eukaryotic Fibrillarin interacting with Nop56
RT amino-terminal domain.";
RL RNA 27:496-512(2021).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has
CC the ability to methylate both RNAs and proteins. Involved in pre-rRNA
CC processing by catalyzing the site-specific 2'-hydroxyl methylation of
CC ribose moieties in pre-ribosomal RNA (PubMed:2686980, PubMed:1825809,
CC PubMed:12215523). Site specificity is provided by a guide RNA that base
CC pairs with the substrate (PubMed:2686980, PubMed:1825809). Methylation
CC occurs at a characteristic distance from the sequence involved in base
CC pairing with the guide RNA (PubMed:2686980, PubMed:1825809). Involved
CC in the biogenesis of the 18S rRNA (PubMed:2686980, PubMed:1825809).
CC Also acts as a protein methyltransferase by mediating methylation of
CC 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs
CC binding of the FACT complex and is specifically present at 35S
CC ribosomal DNA locus (PubMed:24352239). {ECO:0000269|PubMed:12215523,
CC ECO:0000269|PubMed:1825809, ECO:0000269|PubMed:24352239,
CC ECO:0000269|PubMed:2686980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) +
CC N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC Evidence={ECO:0000269|PubMed:24352239};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000269|PubMed:12215523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48629;
CC Evidence={ECO:0000269|PubMed:12215523};
CC -!- SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein
CC (snoRNP) particles that contain SNU13, NOP1, SIK1/NOP56 and NOP58, plus
CC a guide RNA. Interacts with snoRNA U3. Interacts with MPP10, NOP58,
CC SIK1 and SOF1. Component of the ribosomal small subunit (SSU)
CC processome composed of at least 40 protein subunits and snoRNA U3.
CC {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:2686980,
CC ECO:0000269|PubMed:8508778, ECO:0000269|PubMed:9372940}.
CC -!- INTERACTION:
CC P15646; P38333: ENP1; NbExp=4; IntAct=EBI-6838, EBI-6482;
CC P15646; P25586: KRR1; NbExp=4; IntAct=EBI-6838, EBI-21773;
CC P15646; Q12460: NOP56; NbExp=5; IntAct=EBI-6838, EBI-17148;
CC P15646; Q12499: NOP58; NbExp=4; IntAct=EBI-6838, EBI-12126;
CC P15646; P39990: SNU13; NbExp=6; IntAct=EBI-6838, EBI-12032;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12756332,
CC ECO:0000269|PubMed:2298745, ECO:0000269|PubMed:2686980}. Note=Fibrillar
CC region of the nucleolus.
CC -!- PTM: Methylated by HMT1, forming asymmetric dimethylarginines (DMA)
CC within a domain referred to as an RGG box, made up of repeated Gly-Gly
CC dipeptides interspersed with Arg and aromatic residues.
CC {ECO:0000269|PubMed:12756332}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J05230; AAA34816.1; -; Genomic_DNA.
DR EMBL; Z48432; CAA88345.1; -; Genomic_DNA.
DR EMBL; Z74061; CAA98571.1; -; Genomic_DNA.
DR EMBL; Z74062; CAA98572.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11835.1; -; Genomic_DNA.
DR PIR; S25421; S25421.
DR RefSeq; NP_010270.1; NM_001180073.1.
DR PDB; 5WLC; EM; 3.80 A; SC/SD=1-327.
DR PDB; 5WYJ; EM; 8.70 A; 3B/3C=1-327.
DR PDB; 5WYK; EM; 4.50 A; 3B/3C=1-327.
DR PDB; 6KE6; EM; 3.40 A; 3B/3C=1-327.
DR PDB; 6LQP; EM; 3.20 A; 3B/3C=1-327.
DR PDB; 6LQQ; EM; 4.10 A; 3B/3C=1-327.
DR PDB; 6LQR; EM; 8.60 A; 3B/3C=1-327.
DR PDB; 6LQS; EM; 3.80 A; 3B/3C=1-327.
DR PDB; 6LQT; EM; 4.90 A; 3B/3C=1-327.
DR PDB; 6LQU; EM; 3.70 A; 3B/3C=1-327.
DR PDB; 6LQV; EM; 4.80 A; 3B/3C=1-327.
DR PDB; 6ND4; EM; 4.30 A; c/d=1-327.
DR PDB; 6ZDT; X-ray; 1.71 A; A=83-327.
DR PDB; 6ZQA; EM; 4.40 A; CA/CB=1-327.
DR PDB; 6ZQB; EM; 3.90 A; CA/CB=1-327.
DR PDB; 6ZQC; EM; 3.80 A; CA/CB=1-327.
DR PDB; 6ZQD; EM; 3.80 A; CA/CB=1-327.
DR PDB; 6ZQE; EM; 7.10 A; CA/CB=1-327.
DR PDB; 7AJT; EM; 4.60 A; CA/CB=1-327.
DR PDB; 7AJU; EM; 3.80 A; CA/CB=1-327.
DR PDB; 7D4I; EM; 4.00 A; 3B/3C=1-327.
DR PDB; 7D5S; EM; 4.60 A; 3B/3C=1-327.
DR PDB; 7D5T; EM; 6.00 A; 3B/3C=1-327.
DR PDB; 7D63; EM; 12.30 A; 3B/3C=1-327.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ND4; -.
DR PDBsum; 6ZDT; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P15646; -.
DR SMR; P15646; -.
DR BioGRID; 32040; 407.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR ComplexPortal; CPX-729; Box C/D snoRNP complex.
DR DIP; DIP-698N; -.
DR IntAct; P15646; 72.
DR MINT; P15646; -.
DR STRING; 4932.YDL014W; -.
DR iPTMnet; P15646; -.
DR MaxQB; P15646; -.
DR PaxDb; P15646; -.
DR PRIDE; P15646; -.
DR EnsemblFungi; YDL014W_mRNA; YDL014W; YDL014W.
DR GeneID; 851548; -.
DR KEGG; sce:YDL014W; -.
DR SGD; S000002172; NOP1.
DR VEuPathDB; FungiDB:YDL014W; -.
DR eggNOG; KOG1596; Eukaryota.
DR GeneTree; ENSGT00550000074792; -.
DR HOGENOM; CLU_059055_1_0_1; -.
DR OMA; GVDQIYM; -.
DR BioCyc; YEAST:G3O-29444-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P15646; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P15646; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0031428; C:box C/D RNP complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; EXP:Reactome.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IDA:SGD.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IDA:ComplexPortal.
DR GO; GO:1990258; P:histone glutamine methylation; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0000451; P:rRNA 2'-O-methylation; TAS:Reactome.
DR GO; GO:0031167; P:rRNA methylation; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0043144; P:sno(s)RNA processing; IMP:SGD.
DR GO; GO:0000452; P:snoRNA guided rRNA 2'-O-methylation; IDA:ComplexPortal.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
DR InterPro; IPR000692; Fibrillarin.
DR InterPro; IPR020813; Fibrillarin_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01269; Fibrillarin; 1.
DR PIRSF; PIRSF006540; Nop17p; 1.
DR PRINTS; PR00052; FIBRILLARIN.
DR SMART; SM01206; Fibrillarin; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00566; FIBRILLARIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isopeptide bond; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation.
FT CHAIN 1..327
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148527"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 8..83
FT /note="RGG-box"
FT REGION 22..42
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT REGION 58..75
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT REGION 179..180
FT /note="S-adenosyl-L-methionine binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y9U3"
FT REGION 198..199
FT /note="S-adenosyl-L-methionine binding"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT REGION 223..224
FT /note="S-adenosyl-L-methionine binding"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT REGION 243..246
FT /note="S-adenosyl-L-methionine binding"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT REGION 281..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 8
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 8
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 12
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 12
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 16
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 16
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 22
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 22
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 26
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 30
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 34
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 34
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 40
FT /note="Omega-N-methylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 48
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26081071, ECO:0000305|PubMed:12756332"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26081071, ECO:0000305|PubMed:12756332"
FT MOD_RES 52
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 58
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26081071, ECO:0000305|PubMed:12756332"
FT MOD_RES 62
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 66
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 66
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 70
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 70
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26046779, ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 73
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 73
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26046779, ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 81
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 81
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23865587,
FT ECO:0000269|PubMed:26046779, ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 87
FT /note="V->D: In nop1.3; thermosensitive allele showing a
FT decrease in histone-glutamine N-methyltransferase activity
FT upon shift to restrictive temperature; when associated with
FT G-103; V-175 and S-219."
FT /evidence="ECO:0000269|PubMed:24352239"
FT MUTAGEN 103
FT /note="E->G: In nop1.3; thermosensitive allele showing a
FT decrease in histone-glutamine N-methyltransferase activity
FT upon shift to restrictive temperature; when associated with
FT D-87; V-175 and S-219."
FT /evidence="ECO:0000269|PubMed:24352239"
FT MUTAGEN 175
FT /note="A->V: In nop1.3; thermosensitive allele showing a
FT decrease in histone-glutamine N-methyltransferase activity
FT upon shift to restrictive temperature; when associated with
FT D-87; G-103 and S-219."
FT /evidence="ECO:0000269|PubMed:24352239"
FT MUTAGEN 219
FT /note="P->S: In nop1.3; thermosensitive allele showing a
FT decrease in histone-glutamine N-methyltransferase activity
FT upon shift to restrictive temperature; when associated with
FT D-87; G-103 and V-175."
FT /evidence="ECO:0000269|PubMed:24352239"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 261..272
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6ZDT"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:6ZDT"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6ZDT"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:6ZDT"
SQ SEQUENCE 327 AA; 34465 MW; 56A8B958A7B6066E CRC64;
MSFRPGSRGG SRGGSRGGFG GRGGSRGGAR GGSRGGFGGR GGSRGGARGG SRGGFGGRGG
SRGGARGGSR GGRGGAAGGA RGGAKVVIEP HRHAGVYIAR GKEDLLVTKN MAPGESVYGE
KRISVEEPSK EDGVPPTKVE YRVWNPFRSK LAAGIMGGLD ELFIAPGKKV LYLGAASGTS
VSHVSDVVGP EGVVYAVEFS HRPGRELISM AKKRPNIIPI IEDARHPQKY RMLIGMVDCV
FADVAQPDQA RIIALNSHMF LKDQGGVVIS IKANCIDSTV DAETVFAREV QKLREERIKP
LEQLTLEPYE RDHCIVVGRY MRSGLKK
